Analytical Data
-
Gene name
ST1
- Application
-
Alternative Names
ST1；STM；Sulfotransferase 1A3
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0DMM9
-
Expression Region
1-295aa
-
AA Sequence
MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL
-
Molecular Weight
50.2kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ST1 recombinant protein has garnered significant attention in recent years due to its potential applications in various fields, particularly in biotechnology and therapeutics. This protein, initially identified in a specific organism, exhibits unique structural and functional properties that suggest its usefulness in several biological processes. Researchers have been focusing on characterizing its molecular features, understanding its role in cellular functions, and exploring its interactions with other biomolecules. The ability to produce ST1 as a recombinant protein enhances its availability for experimental studies, allowing scientists to investigate its mechanisms of action in greater detail. Furthermore, the versatility of recombinant protein technology facilitates modifications that can enhance ST1's stability and efficacy, paving the way for potential applications in drug development or as a biosensor. The ongoing research aims to elucidate the biological significance of ST1, assess its therapeutic potential, and ultimately translate these findings into practical solutions for health and disease management. As interest in protein-based therapies continues to grow, ST1 stands out as a promising candidate that could contribute to advancements in medical science and biotechnology.
